Ubiquitous carbohydrate binding modules decorate 936 lactococcal siphophage virions

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dc.contributor.authorHayes, Stephen
dc.contributor.authorMahony, Jennifer
dc.contributor.authorVincentelli, Renaud
dc.contributor.authorRamond, Laurie
dc.contributor.authorNauta, Arjen
dc.contributor.authorvan Sinderen, Douwe
dc.contributor.authorCambillau, Christian
dc.contributor.funderIrish Research Councilen
dc.contributor.funderScience Foundation Irelanden
dc.contributor.funderFrench Infrastructure for Integrated Structural Biologyen
dc.date.accessioned2019-10-23T04:34:10Z
dc.date.available2019-10-23T04:34:10Z
dc.date.issued2019-07-09
dc.description.abstractWith the availability of an increasing number of 3D structures of bacteriophage components, combined with powerful in silico predictive tools, it has become possible to decipher the structural assembly and functionality of phage adhesion devices. In the current study, we examined 113 members of the 936 group of lactococcal siphophages, and identified a number of Carbohydrate Binding Modules (CBMs) in the neck passage structure and major tail protein, on top of evolved Dit proteins, as recently reported by us. The binding ability of such CBM-containing proteins was assessed through the construction of green fluorescent protein fusion proteins and subsequent binding assays. Two CBMs, one from the phage tail and another from the neck, demonstrated definite binding to their phage-specific host. Bioinformatic analysis of the structural proteins of 936 phages reveals that they incorporate binding modules which exhibit structural homology to those found in other lactococcal phage groups and beyond, indicating that phages utilize common structural “bricks” to enhance host binding capabilities. The omnipresence of CBMs in Siphophages supports their beneficial role in the infection process, as they can be combined in various ways to form appendages with different shapes and functionalities, ensuring their success in host detection in their respective ecological niches.en
dc.description.sponsorshipFrench Infrastructure for Integrated Structural Biology (FRISBI ANR-10-INSB-05-01)en
dc.description.statusPeer revieweden
dc.description.versionPublished Versionen
dc.format.mimetypeapplication/pdfen
dc.identifier.articleid631en
dc.identifier.citationHayes, S., Mahony, J., Vincentelli, R., Ramond, L., Nauta, A., van Sinderen, D. and Cambillau, C. (2019) 'Ubiquitous Carbohydrate Binding Modules Decorate 936 Lactococcal Siphophage Virions', Viruses, 11(7), 631. (19pp.) DOI: 10.3390/v11070631en
dc.identifier.doi10.3390/v11070631en
dc.identifier.eissn1999-4915
dc.identifier.endpage19en
dc.identifier.issued7en
dc.identifier.journaltitleVirusesen
dc.identifier.startpage1en
dc.identifier.urihttps://hdl.handle.net/10468/8829
dc.identifier.volume11en
dc.language.isoenen
dc.publisherMDPI AGen
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Starting Investigator Research Grant (SIRG)/15/SIRG/3430/IE/Phage-host interactome of the dairy bacterium Streptococcus thermophilus (PHIST)/en
dc.relation.projectinfo:eu-repo/grantAgreement/SFI/SFI Investigator Programme/13/IA/1953/IE/Functional analysis of the host adsorption and DNA injection processes of a lactococcal bacteriophage/en
dc.relation.urihttps://www.mdpi.com/1999-4915/11/7/631/htm
dc.rights© 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).en
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/en
dc.subjectBacteriophageen
dc.subjectLactococcus lactisen
dc.subjectReceptor-binding proteinen
dc.subjectCarbohydrate binding moduleen
dc.subjectPhage-host interactionsen
dc.titleUbiquitous carbohydrate binding modules decorate 936 lactococcal siphophage virionsen
dc.typeArticle (peer-reviewed)en
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